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BMPER encodes a secreted protein that interacts with, and inhibits bone morphogenetic protein (BMP) function. Additionally we are shipping BMPER Kits (11) and BMPER Proteins (3) and many more products for this protein.
Showing 10 out of 30 products:
Chicken Polyclonal BMPER Primary Antibody for IHC, WB - ABIN2784992
Binnerts, Wen, Canté-Barrett, Bright, Chen, Asundi, Sattari, Tang, Boyle, Funk, Rupp: Human Crossveinless-2 is a novel inhibitor of bone morphogenetic proteins. in Biochemical and biophysical research communications 2004
The bone morphogenetic protein- binding protein Cv-2 negatively regulates bone morphogenetic protein signaling.
Cv-2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling.
The NMR structure of the Danio rerio CV2 VWC1 (show VWCE Antibodies) domain in its unbound state shows the key features for high affinity binding to BMP-2 (show BMP4 Antibodies) are a pre-oriented peptide loop.
Crossveinless 2 functions in a positive-feedback loop to locally enhance BMP activity and is required for neural crest fate determination.
LRP1 (show LRP1 Antibodies) acts as an endocytic receptor for Bmper and a coreceptor of Bmp4 (show BMP4 Antibodies) to mediate the endocytosis of the Bmper/Bmp4 (show BMP4 Antibodies) signaling complex.
Binding of CV2 to Chordin (show CHRD Antibodies) promotes BMP-2 (show BMP4 Antibodies) signaling.
Cvl2 was identified as an essential pro-bone morphogenetic protein factor during zebrafish embryogenesis.
Bmper is a conserved regulator of hematopoietic and vascular development in zebrafish.
Initial crystallographic analysis suggests that a complete binary complex consisting of one BMP2 (show BMP4 Antibodies) dimer bound to two crossveinless 2 (CV2) von Willebrand type C (VWC1 (show VWCE Antibodies)) domains is present in the asymmetric unit.
The structure of the complex between CV-2 Von Willebrand factor (show VWF Antibodies) type C (VWC) domain 1 and BMP-2 (show BMP4 Antibodies), is reported.
CV2/Chordin interaction may help coordinate bone morphogenetic protein (BMP) diffusion to the ventral side of the embryo, ensuring that BMPs liberated from Chordin inhibition by tolloid proteolysis cause peak signaling levels.
BMPER variants associated with a novel, attenuated subtype of diaphanospondylodysostosis.
BMPER-dependent pathway involved in high glucose induced alkaline phosphatase expression in vascular smooth muscle cells.
The proangiogenic BMPER effect in endothelial cells is mediated by inhibition of antiangiogenic thrombospondin-1 (show THBS1 Antibodies) and enhanced expression and activation of the FGF signaling pathway that is crucial in the promotion of angiogenesis.
these results suggest that BMPER and Tsg maintain a fine-tuned equilibrium that controls BMP pathway activity and is necessary for vascular cell homeostasis.
BMPER is a novel regulator of the osteoblast-like differentiation of HCASMCs.
Bmper is a critical regulator of Bmp-mediated vascular inflammation and that the fine-tuning of Bmp and Bmper levels is essential in the maintenance of normal vascular homeostasis.
The data unequivocally demonstrated that BMPER is highly expressed in malignant tumors and that the growth of lung, colon, and uterine carcinomas is dependent on the presence of BMPER.
Mutual regulation by BMP-9 (show GDF2 Antibodies) and CV2 is essential in regulating the development of the vascular endothelium.
Diaphonospondylodysostosis is caused by loss of BMPER function.
BMPER-mediated signaling plays an essential role in vertebral segmentation early in human development, while defects in BMPER produce Diaphanospondylodysostosis.
Results identified variant SNPs in BMPER gene associated with phenotypic variation in cattle that can be used as genetic markers for breeding.
BMPER promoter polymorphisms have an effect on the intramuscular fat deposition in longissimus dorsi muscle content.
BMPER-induced BMP signaling promotes coronary artery remodeling.
BMPER appears to play a role in regulating both vessel density and cardiac development
BMPER expression is decreased following lung injury, which in turn impairs epithelial integrity, characterized by reduction of E-cadherin (show CDH1 Antibodies) and epithelial leakage in vitro and in vivo.
Bmper may play an important role in suppressing hepcidin (show HAMP Antibodies) production in hypotransferrinemic mice.
BMP modulator BMPER is a new protective regulator of vascular inflammation that modulates leukocyte adhesion and migration in vitro and in vivo.
BMPER is important in the regulation of BMP signaling and revascularization in the hypoxic retina.
The data indicate a role for CV2 and Chd in the establishment of the vertebral morphogenetic field through the long-range relocalization of Chd/BMP complexes.
This gene encodes a secreted protein that interacts with, and inhibits bone morphogenetic protein (BMP) function. It has been shown to inhibit BMP2- and BMP4-dependent osteoblast differentiation and BMP-dependent differentiation of the chondrogenic cells. Mutations in this gene are associated with a lethal skeletal disorder, diaphanospondylodysostosis.
BMP-binding endothelial regulator precursor protein
, BMP binding endothelial regulator
, crossveinless 2
, BMP-binding endothelial regulator protein-like
, BMP-binding endothelial regulator protein
, bone morphogenetic protein-binding endothelial cell precursor-derived regulator